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ARNF_YERPS
ID   ARNF_YERPS              Reviewed;         128 AA.
AC   Q93PD4; Q66A08;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnF {ECO:0000255|HAMAP-Rule:MF_00538};
DE            Short=L-Ara4N-phosphoundecaprenol flippase subunit ArnF {ECO:0000255|HAMAP-Rule:MF_00538};
DE   AltName: Full=Undecaprenyl phosphate-aminoarabinose flippase subunit ArnF {ECO:0000255|HAMAP-Rule:MF_00538};
GN   Name=arnF {ECO:0000255|HAMAP-Rule:MF_00538}; OrderedLocusNames=YPTB2324;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=32777 / IP2777 / Serotype O1:b;
RX   PubMed=15583148; DOI=10.1099/mic.0.27426-0;
RA   Marceau M.B., Sebbane F., Ewann F., Collyn F., Lindner B., Campos M.A.,
RA   Bengoechea J.-A., Simonet M.;
RT   "The pmrF polymyxin-resistance operon of Yersinia pseudotuberculosis is
RT   upregulated by the PhoP-PhoQ two-component system but not by PmrA-PmrB, and
RT   is not required for virulence.";
RL   Microbiology 150:3947-3957(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC   -!- FUNCTION: Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol
CC       (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the
CC       periplasmic side of the inner membrane. {ECO:0000255|HAMAP-
CC       Rule:MF_00538}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00538}.
CC   -!- SUBUNIT: Heterodimer of ArnE and ArnF. {ECO:0000255|HAMAP-
CC       Rule:MF_00538}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00538}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00538}.
CC   -!- INDUCTION: Activated by low magnesium concentrations, via the two-
CC       component regulatory system PhoP/PhoQ. {ECO:0000269|PubMed:15583148}.
CC   -!- SIMILARITY: Belongs to the ArnF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00538}.
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DR   EMBL; AF336802; AAK69646.1; -; Genomic_DNA.
DR   EMBL; BX936398; CAH21562.1; -; Genomic_DNA.
DR   RefSeq; WP_002211819.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q93PD4; -.
DR   EnsemblBacteria; CAH21562; CAH21562; YPTB2324.
DR   GeneID; 66841242; -.
DR   KEGG; ypo:BZ17_130; -.
DR   KEGG; yps:YPTB2324; -.
DR   PATRIC; fig|273123.14.peg.139; -.
DR   OMA; AQLGMRW; -.
DR   UniPathway; UPA00030; -.
DR   Proteomes; UP000001011; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:1901505; F:carbohydrate derivative transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR   HAMAP; MF_00538; Flippase_ArnF; 1.
DR   InterPro; IPR022832; Flippase_ArnF.
DR   InterPro; IPR000390; Small_drug/metabolite_transptr.
DR   PANTHER; PTHR30561; PTHR30561; 1.
PE   2: Evidence at transcript level;
KW   Cell inner membrane; Cell membrane; Lipid A biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism; Lipopolysaccharide biosynthesis;
KW   Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..128
FT                   /note="Probable 4-amino-4-deoxy-L-arabinose-
FT                   phosphoundecaprenol flippase subunit ArnF"
FT                   /id="PRO_0000218161"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00538"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00538"
FT   TOPO_DOM        32..47
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00538"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00538"
FT   TOPO_DOM        69..77
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00538"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00538"
FT   TOPO_DOM        99..101
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00538"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00538"
FT   TOPO_DOM        123..128
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00538"
FT   CONFLICT        56
FT                   /note="M -> I (in Ref. 1; AAK69646)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        59
FT                   /note="A -> S (in Ref. 1; AAK69646)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   128 AA;  14223 MW;  33AC97482B8E21B4 CRC64;
     MKGYLWGGAS VVLVTVAQLV LKWGMMNIPL LSLADINVQF LTMYFVQLAS VMCGLMGYAL
     SMLCWFFALR YLPLNRAYPL LSLSYALVYL GAVLLPWFNE PATLLKTLGA GFILLGIWLI
     NIKPIKAS
 
 
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